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Vibrational IR-emission spectra of bacteriorhodopsin (bR) were recorded under continuous illumination with visible light at room temperature. They contain selective information about the chromophore, Schiff base, and opsin. The spectral bands were identified by comparing the data with resonance Raman and IR absorption data. The IR-emission spectra were shown to contain a set of bands characteristic for both all-trans (bR568) and 13-cis conformations (K610-like intermediate) simultaneously. Variation of spectral composition and the intensity of visible light illumination influenced the spectral traces and intensity distribution between them. Greater intensity of deformational vibrations suggests distorted retinal structure in the vibrationally excited ground electronic state. The origin of the emitting species of bR is discussed.

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